Point mutation in cytochrome b of yeast ubihydroquinone:cytochrome-c oxidoreductase causing myxothiazol resistance and facilitated dissociation of the iron-sulfur subunit.

doi:10.1111/j.1432-1033.1992.tb17197.x

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Article

Point mutation in cytochrome b of yeast ubihydroquinone:cytochrome-c oxidoreductase causing myxothiazol resistance and facilitated dissociation of the iron-sulfur subunit.

European journal of biochemistry - 1 Sept 1992

Geier B M, Schägger H, Brandt U, Colson A M, Von Jagow G

Abstract excerpt

Cytochrome-c reductase was isolated from Saccharomyces cerevisiae GM50-3C. A tenth subunit was detected with molecular mass 8.5 kDa on SDS/PAGE. Two yeast mutants selected for resistance to myxothiazol, an inhibitor of the Q0 center (Q, ubiquinone) of cytochrome-c reductase, were analysed. The single amino acid substitution in the cytochrome-b subunit, N256Y in the mutant Myx-119 and G137R in the mutant Myx-118,...

Topics

Amino Acid Sequence
Catalysis
Cytochrome b Group
Drug Resistance, Microbial
Electron Transport Complex III
Electrophoresis, Polyacrylamide Gel
Intracellular Membranes
Iron-Sulfur Proteins
Kinetics
Methacrylates

Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

Mitochondria

Molecular Sequence Data

Mutation

Peptide Fragments

Saccharomyces cerevisiae

Spectrometry, Fluorescence

Thiazoles

Source

Open in PubMed

Identifiers

PMID: 1325905
DOI: 10.1111/j.1432-1033.1992.tb17197.x

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 29 Aug 2026. Prepared record publication-1325905-2026-08-29.1. Manifest publication-graph-cohort-2026-08-29.1.

Source receipt: PubMed via Helena Literature Corpus, retrieved 29 Aug 2026.

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